A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Serine and threonine residues of plant STN7 kinase are differentially phosphorylated upon changing light conditions and specifically influence the activity and stability of the kinase
Tekijät: Trotta Andrea, Suorsa Marjaana, Rantala Marjaana, Lundin Björn, Aro Eva-Mari
Kustantaja: WILEY-BLACKWELL
Julkaisuvuosi: 2016
Journal: Plant Journal
Tietokannassa oleva lehden nimi: PLANT JOURNAL
Lehden akronyymi: PLANT J
Vuosikerta: 87
Numero: 5
Aloitussivu: 484
Lopetussivu: 494
Sivujen määrä: 11
ISSN: 0960-7412
eISSN: 1365-313X
DOI: https://doi.org/10.1111/tpj.13213
Verkko-osoite: http://onlinelibrary.wiley.com/doi/10.1111/tpj.13213/full
Rinnakkaistallenteen osoite: https://research.utu.fi/converis/portal/detail/Publication/18133624
STN7 kinase catalyzes the phosphorylation of the globally most common membrane proteins, the light-harvesting complex II (LHCII) in plant chloroplasts. STN7 itself possesses one serine (Ser) and two threonine (Thr) phosphosites. We show that phosphorylation of the Thr residues protects STN7 against degradation in darkness, low light and red light, whereas increasing light intensity and far red illumination decrease phosphorylation and induce STN7 degradation. Ser phosphorylation, in turn, occurs under red and low intensity white light, coinciding with the client protein (LHCII) phosphorylation. Through analysis of the counteracting LHCII phosphatase mutant tap38/pph1, we show that Ser phosphorylation and activation of the STN7 kinase for subsequent LHCII phosphorylation are heavily affected by pre-illumination conditions. Transitions between the three activity states of the STN7 kinase (deactivated in darkness and far red light, activated in low and red light, inhibited in high light) are shown to modulate the phosphorylation of the STN7 Ser and Thr residues independently of each other. Such dynamic regulation of STN7 kinase phosphorylation is crucial for plant growth and environmental acclimation.
Ladattava julkaisu This is an electronic reprint of the original article. |  |
